This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Carson, M J
Right arrow Articles by Beckwith, J
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Carson, M J
Right arrow Articles by Beckwith, J

 Previous Article  |  Next Article 

J Bacteriol. 1991 April; 173(7): 2187-2195

research-article

The FtsQ protein of Escherichia coli: membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations.

M J Carson, J Barondess and J Beckwith

Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115.

ABSTRACT

The ftsQ gene is one of several genes thought to be specifically required for septum formation in Escherichia coli. Published work on the cell division behavior of ftsQ temperature-sensitive mutants suggested that the FtsQ product is required throughout the whole process of septum formation. Here we provide additional support for this hypothesis based on microscopic observations of the cell division defects resulting from insertional and temperature-sensitive mutations in the ftsQ gene, and constitutive overexpression of its gene product. On the basis of the published, predicted amino acid sequence of the FtsQ protein and our analysis of fusion proteins of the FtsQ protein to bacterial alkaline phosphatase, we conclude that FtsQ is a simple cytoplasmic membrane protein with a approximately 25-amino-acid cytoplasmic domain and a approximately 225-amino-acid periplasmic domain. We estimate that the FtsQ protein is present at about 22 copies per cell.


J Bacteriol. 1991 April; 173(7): 2187-2195




This article has been cited by other articles:

  • Masson, S., Kern, T., Le Gouellec, A., Giustini, C., Simorre, J.-P., Callow, P., Vernet, T., Gabel, F., Zapun, A. (2009). Central Domain of DivIB Caps the C-terminal Regions of the FtsL/DivIC Coiled-coil Rod. J. Biol. Chem. 284: 27687-27700 [Abstract] [Full Text]  
  • Arends, S. J. R., Kustusch, R. J., Weiss, D. S. (2009). ATP-Binding Site Lesions in FtsE Impair Cell Division. J. Bacteriol. 191: 3772-3784 [Abstract] [Full Text]  
  • Peterson, J. M., Phillips, G. J. (2008). Characterization of Conserved Bases in 4.5S RNA of Escherichia coli by Construction of New F' Factors. J. Bacteriol. 190: 7709-7718 [Abstract] [Full Text]  
  • Le Gouellec, A., Roux, L., Fadda, D., Massidda, O., Vernet, T., Zapun, A. (2008). Roles of Pneumococcal DivIB in Cell Division. J. Bacteriol. 190: 4501-4511 [Abstract] [Full Text]  
  • Joseleau-Petit, D., Liebart, J.-C., Ayala, J. A., D'Ari, R. (2007). Unstable Escherichia coli L Forms Revisited: Growth Requires Peptidoglycan Synthesis. J. Bacteriol. 189: 6512-6520 [Abstract] [Full Text]  
  • D'Ulisse, V., Fagioli, M., Ghelardini, P., Paolozzi, L. (2007). Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins. Microbiology 153: 124-138 [Abstract] [Full Text]  
  • Goehring, N. W., Gueiros-Filho, F., Beckwith, J. (2005). Premature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli. Genes Dev. 19: 127-137 [Abstract] [Full Text]  
  • Ursinus, A., van den Ent, F., Brechtel, S., de Pedro, M., Holtje, J.-V., Lowe, J., Vollmer, W. (2004). Murein (Peptidoglycan) Binding Property of the Essential Cell Division Protein FtsN from Escherichia coli. J. Bacteriol. 186: 6728-6737 [Abstract] [Full Text]  
  • Errington, J., Daniel, R. A., Scheffers, D.-J. (2003). Cytokinesis in Bacteria. Microbiol. Mol. Biol. Rev. 67: 52-65 [Abstract] [Full Text]  
  • Buddelmeijer, N., Judson, N., Boyd, D., Mekalanos, J. J., Beckwith, J. (2002). YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site. Proc. Natl. Acad. Sci. USA 99: 6316-6321 [Abstract] [Full Text]  
  • Chen, J. C., Minev, M., Beckwith, J. (2002). Analysis of ftsQ Mutant Alleles in Escherichia coli: Complementation, Septal Localization, and Recruitment of Downstream Cell Division Proteins. J. Bacteriol. 184: 695-705 [Abstract] [Full Text]  
  • Katis, V. L., Wake, R. G. (1999). Membrane-Bound Division Proteins DivIB and DivIC of Bacillus subtilis Function Solely through Their External Domains in both Vegetative and Sporulation Division. J. Bacteriol. 181: 2710-2718 [Abstract] [Full Text]  
  • Chen, J. C., Weiss, D. S., Ghigo, J.-M., Beckwith, J. (1999). Septal Localization of FtsQ, an Essential Cell Division Protein in Escherichia coli. J. Bacteriol. 181: 521-530 [Abstract] [Full Text]  
  • Joseleau-Petit, D., Vinella, D., D'Ari, R. (1999). Metabolic Alarms and Cell Division in Escherichia coli. J. Bacteriol. 181: 9-14 [Full Text]  
  • Buddelmeijer, N., Aarsman, M. E. G., Kolk, A. H. J., Vicente, M., Nanninga, N. (1998). Localization of Cell Division Protein FtsQ by Immunofluorescence Microscopy in Dividing and Nondividing Cells of Escherichia coli. J. Bacteriol. 180: 6107-6116 [Abstract] [Full Text]  
  • Goffin, C., Ghuysen, J.-M. (1998). Multimodular Penicillin-Binding Proteins: An Enigmatic Family of Orthologs and Paralogs. Microbiol. Mol. Biol. Rev. 62: 1079-1093 [Abstract] [Full Text]  
  • Nanninga, N. (1998). Morphogenesis of Escherichia coli. Microbiol. Mol. Biol. Rev. 62: 110-129 [Abstract] [Full Text]  
  • Pogliano, J., Pogliano, K., Weiss, D. S., Losick, R., Beckwith, J. (1997). Inactivation of FtsI inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites. Proc. Natl. Acad. Sci. USA 94: 559-564 [Abstract] [Full Text]  
  • Tian, H., Boyd, D., Beckwith, J. (2000). A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery. Proc. Natl. Acad. Sci. USA 97: 4730-4735 [Abstract] [Full Text]  
  • Buddelmeijer, N., Judson, N., Boyd, D., Mekalanos, J. J., Beckwith, J. (2002). YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site. Proc. Natl. Acad. Sci. USA 99: 6316-6321 [Abstract] [Full Text]